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P37617 (ATZN_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lead, cadmium, zinc and mercury-transporting ATPase

EC=3.6.3.3
EC=3.6.3.5
Gene names
Name:zntA
Synonyms:yhhO
Ordered Locus Names:b3469, JW3434
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length732 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in export of lead, cadmium, zinc and mercury.

Catalytic activity

ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out).

ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out).

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 1 HMA domain.

Ontologies

Keywords
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Cadmium
Magnesium
Mercury
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence alignment Ref.4. Source: GOC

cadmium ion transmembrane transport

Inferred from direct assay Ref.6. Source: GOC

cobalt ion transport

Inferred from mutant phenotype Ref.5. Source: EcoCyc

detoxification of zinc ion

Inferred from mutant phenotype Ref.4. Source: EcoliWiki

lead ion transport

Inferred from mutant phenotype PubMed 9830000. Source: EcoCyc

nickel cation transmembrane transport

Inferred from mutant phenotype Ref.5. Source: GOC

response to cadmium ion

Inferred from mutant phenotype Ref.4. Source: EcoliWiki

zinc ion transmembrane transport

Inferred from direct assay Ref.6. Source: GOC

zinc ion transport

Inferred from mutant phenotype Ref.4. Source: EcoliWiki

   Cellular_componentintegral component of membrane

Inferred from direct assay Ref.4. Source: EcoCyc

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from sequence alignment Ref.4. Source: EcoliWiki

cadmium-exporting ATPase activity

Inferred from direct assay Ref.6. Source: EcoCyc

cobalt ion transmembrane transporter activity

Inferred from mutant phenotype Ref.5. Source: EcoCyc

lead ion transmembrane transporter activity

Inferred from mutant phenotype Ref.5. Source: EcoCyc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nickel cation transmembrane transporter activity

Inferred from mutant phenotype Ref.5. Source: EcoCyc

zinc-exporting ATPase activity

Inferred from direct assay Ref.6. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 732732Lead, cadmium, zinc and mercury-transporting ATPase
PRO_0000046332

Regions

Topological domain1 – 124124Periplasmic Potential
Transmembrane125 – 14521Helical; Potential
Topological domain146 – 19146Cytoplasmic Potential
Transmembrane192 – 21221Helical; Potential
Topological domain213 – 356144Periplasmic Potential
Transmembrane357 – 37721Helical; Potential
Topological domain378 – 3836Cytoplasmic Potential
Transmembrane384 – 40421Helical; Potential
Topological domain405 – 46157Periplasmic Potential
Transmembrane462 – 48221Helical; Potential
Topological domain483 – 632150Cytoplasmic Potential
Transmembrane633 – 65321Helical; Potential
Topological domain654 – 69340Periplasmic Potential
Transmembrane694 – 71421Helical; Potential
Topological domain715 – 73218Cytoplasmic Potential
Domain49 – 11365HMA

Sites

Active site43614-aspartylphosphate intermediate By similarity
Metal binding581Zinc
Metal binding591Zinc
Metal binding621Zinc
Metal binding6281Magnesium By similarity
Metal binding6321Magnesium By similarity

Secondary structure

............. 732
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37617 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 25476EA830786465

FASTA73276,840
        10         20         30         40         50         60 
MSTPDNHGKK APQFAAFKPL TTVQNANDCC CDGACSSTPT LSENVSGTRY SWKVSGMDCA 

        70         80         90        100        110        120 
ACARKVENAV RQLAGVNQVQ VLFATEKLVV DADNDIRAQV ESALQKAGYS LRDEQAAEEP 

       130        140        150        160        170        180 
QASRLKENLP LITLIVMMAI SWGLEQFNHP FGQLAFIATT LVGLYPIARQ ALRLIKSGSY 

       190        200        210        220        230        240 
FAIETLMSVA AIGALFIGAT AEAAMVLLLF LIGERLEGWA ASRARQGVSA LMALKPETAT 

       250        260        270        280        290        300 
RLRKGEREEV AINSLRPGDV IEVAAGGRLP ADGKLLSPFA SFDESALTGE SIPVERATGD 

       310        320        330        340        350        360 
KVPAGATSVD RLVTLEVLSE PGASAIDRIL KLIEEAEERR APIERFIDRF SRIYTPAIMA 

       370        380        390        400        410        420 
VALLVTLVPP LLFAASWQEW IYKGLTLLLI GCPCALVIST PAAITSGLAA AARRGALIKG 

       430        440        450        460        470        480 
GAALEQLGRV TQVAFDKTGT LTVGKPRVTA IHPATGISES ELLTLAAAVE QGATHPLAQA 

       490        500        510        520        530        540 
IVREAQVAEL AIPTAESQRA LVGSGIEAQV NGERVLICAA GKHPADAFTG LINELESAGQ 

       550        560        570        580        590        600 
TVVLVVRNDD VLGVIALQDT LRADAATAIS ELNALGVKGV ILTGDNPRAA AAIAGELGLE 

       610        620        630        640        650        660 
FKAGLLPEDK VKAVTELNQH APLAMVGDGI NDAPAMKAAA IGIAMGSGTD VALETADAAL 

       670        680        690        700        710        720 
THNHLRGLVQ MIELARATHA NIRQNITIAL GLKGIFLVTT LLGMTGLWLA VLADTGATVL 

       730 
VTANALRLLR RR 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase."
Rensing C., Mitra B., Rosen B.P.
Proc. Natl. Acad. Sci. U.S.A. 94:14326-14331(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase."
Beard S.J., Hashim R., Membrillo-Hernandez J., Hughes M.N., Poole R.K.
Mol. Microbiol. 25:883-891(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli."
Sharma R., Rensing C., Rosen B.P., Mitra B.
J. Biol. Chem. 275:3873-3878(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
[8]"A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)."
Banci L., Bertini I., Ciofi-Baffoni S., Finney L.A., Outten C.E., O'Halloran T.V.
J. Mol. Biol. 323:883-897(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 46-118 IN APO AND ZINC-BOUND FORMS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00039 Genomic DNA. Translation: AAB18444.1.
U00096 Genomic DNA. Translation: AAC76494.1.
AP009048 Genomic DNA. Translation: BAE77824.1.
PIRS47688.
RefSeqNP_417926.1. NC_000913.3.
YP_491965.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MWYNMR-A46-118[»]
1MWZNMR-A46-118[»]
ProteinModelPortalP37617.
SMRP37617. Positions 19-732.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-12947N.
IntActP37617. 8 interactions.
MINTMINT-1256950.
STRING511145.b3469.

Protein family/group databases

TCDB3.A.3.6.2. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbP37617.
PRIDEP37617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76494; AAC76494; b3469.
BAE77824; BAE77824; BAE77824.
GeneID12933927.
947972.
KEGGecj:Y75_p3709.
eco:b3469.
PATRIC32122382. VBIEscCol129921_3568.

Organism-specific databases

EchoBASEEB2129.
EcoGeneEG12215. zntA.

Phylogenomic databases

eggNOGCOG2217.
HOGENOMHOG000250399.
KOK01534.
OMALPWIYKG.
OrthoDBEOG6742RM.
PhylomeDBP37617.
ProtClustDBPRK11033.

Enzyme and pathway databases

BioCycEcoCyc:YHHO-MONOMER.
ECOL316407:JW3434-MONOMER.
MetaCyc:YHHO-MONOMER.
SABIO-RKP37617.

Gene expression databases

GenevestigatorP37617.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR027256. Cation_transp_P-typ_ATPase_IB.
IPR001757. Cation_transp_P_typ_ATPase.
IPR027265. Di_cation_transp_P_ATPase.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
PANTHERPTHR24093:SF126. PTHR24093:SF126. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SUPFAMSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP37617.
PROP37617.

Entry information

Entry nameATZN_ECOLI
AccessionPrimary (citable) accession number: P37617
Secondary accession number(s): Q2M7D2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene